ID A0A1K1RMH3_9BACT Unreviewed; 1467 AA.
AC A0A1K1RMH3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05661012_03977 {ECO:0000313|EMBL:SFW73222.1};
OS Chitinophaga sancti.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW73222.1, ECO:0000313|Proteomes:UP000183788};
RN [1] {ECO:0000313|EMBL:SFW73222.1, ECO:0000313|Proteomes:UP000183788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 784 {ECO:0000313|EMBL:SFW73222.1,
RC ECO:0000313|Proteomes:UP000183788};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPIZ01000013; SFW73222.1; -; Genomic_DNA.
DR STRING; 1004.SAMN05661012_03977; -.
DR Proteomes; UP000183788; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 6.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1467
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013199219"
FT TRANSMEM 923..942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 969..1178
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1216..1331
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1363..1462
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT REGION 25..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1264
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1467 AA; 165275 MW; EB86602D207BEFF7 CRC64;
MRLQQYFHLL CGLLLPSLTG LSILSASPVD TNPEKKTRTN TVRETQAGTA RETHTGAASK
TYTNTSREIH TSSPRETHTG TANKTYTNPP GEIHTSSRTN TDPSANIRLE QLTTYDGLSQ
NTVRCLLQDK KGFIWVGTLN GLNRYDGRKF TVYRTNTGIT QPISDNRIRS LYEDKKGIIW
VKTAEGHYHC FDPGKETFIN IIPDSADLTY DHLFETTKGV WLYSKTNGCL HNGRHYNLGS
VHFIFEDSRH TEWIGTDKNL YQLDKQGNAI PLYEGNFIKA ITKAEQLYFI KKQGILIHDL
HTNKCTFNDP LPGTILTDAA ILPNNRILLG TQQDGLKIAD LQNNRLIPTT RLFGEDIPGH
IDIETDQDAG IWVNNHTGNV WYLDPAQAFS QRITLIPASV MKVIDDCRFA FAADHKGKVW
ITTYGGGLYC FDKTNRQLQR FVYDPDNPNG LSTNYLLSVI ADRAGLIWVG AEHTGLQKLT
PQSLHVTHIF PEAQTPERYA ANGVKTIFED SYKRIWVSTR NGALYLYNDH LEKNRSLDHL
LPGQCANIYC MTEDARGYLW IGTKGDGVYI VHRDSLQQKA RHFLLPSRDN RLVYTIMQDR
QQRMWVGTFG SGLYLATYKG GNQLEWQNFF HDGVNPVYIR CLLQDQHNQL WAGTNNGLLV
FNPEHLLAGN NDITTYQAGL GSNEIKSLCE DHKGRIWIGT TGGGFSRFVP QKKTFINYTT
EQGLSHDVVN SMLEDAQGNL WVSTENGLTR FNPEKSTFEV FYFANNPLGN LFSEGACFRR
ENGQLLWGSL NGFYSFFPGQ LKNGNADAPV LLTGLSVAGN PVVLEESIST ARSITLEPGQ
KVFSISFASL ALRNPQQNKY TYILENYEDE WNAPSSYNVA TYRNLPPGKY TFKVRGTNDD
GSWSKHEARI QITVLPPFWR SNVAIMLSLA LIIGMVMCVI VINRRIHRLQ HAVTLEKELT
EYKLNFFTDI SHEFRTPLSL IVSAMEQLIP GKQSGNKHLH IMQRQVAHLM RLADQLLDFR
KIQHKKLQLQ VQETEMIQFI QDICNGFTDL AAQKQITLSF RANVDACMAW VDQGKLDKIL
YNLLSNAHKF TPAGGKIDLL VHIDHQLTIK VVDNGIAISA EKQHMVFQRF TQLNFSPTGT
GLGLSLTKEL VTLHKGTISF ENNADAGVTF TVNLPVHKLA YVADEIVEQT ICKAPVLPFI
DDTDTAAIVA PSSRYSVLII EDNPDISAYL ATTLSRYFHI YTAANGREGL EQAIAQSPDL
IVCDVMLPEM NGLEITHKIR SEFQTCHIPV ILLTALSSGE HQLQGIDAGA DAYITKPFST
RFLLTSIIRI IEQREKIRKR FANDPGFFAV HISENEADQQ FLEKINMIIE KNLDNAQFSV
DDFALAMKMG RTLFYKKVKG LTGYSPNEYI RLVRVKKAAE LLNTGEYTVA EVAYKVGMND
PFYFSKCFKT QFGVPPSVHL KKVKAAG
//